title: Yet another polymorph of α-synuclein: solid-state sequential assignments.
abstract: Parkinson's disease is a neurological human proteinopathy, which is caused by the accumulation of protein aggregates of high molecular mass. α-Synuclein is a major component of these fibrillar, β-sheet rich, insoluble assemblies and is deposited in the form of amyloids. Structural characterization of amyloids is possible by solid-state NMR, although no atomic-resolution structure is available as of today. α-Synuclein, as many other pathology-related fibril-forming proteins, can form a number of different polymorphs that are sometimes tricky to obtain in pure form. Here, we describe the chemical shifts and secondary structure analysis of a polymorph that also adopts mainly β-sheet conformation, with a fibrillar core ranging from residues 38 to 94. In addition, residues 15-20 from the N-terminus found to be part of a rigid ordered β-sheet. The chemical shifts differ substantially from the polymorph we previously assigned.
authors.affiliation: Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Julia
authors.initials: J
authors.lastname: Gath
authors.forename: Luc
authors.initials: L
authors.lastname: Bousset
authors.forename: Birgit
authors.initials: B
authors.lastname: Habenstein
authors.forename: Ronald
authors.initials: R
authors.lastname: Melki
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D051844:alpha-Synuclein